Complex between the pryspry domain of TRIM21 and IgG fc. Determined by X-ray diffraction at 2.35 Å resolution. Released 27 Mar 2007.
Explore 2IWG in 3D Show helices and sheets RCSB PDB PDBe
2IWG contains 25 α-helices and 74 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 239-243 | 5 | 1 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-250 | 4 | |
| β-strand | 258-267 | 10 | 1 |
| β-strand | 274-279 | 6 | 2 |
| β-strand | 283-284 | 2 | 2 |
| β-strand | 288-289 | 2 | 1 |
| α-helix | 290-292 | 3 | |
| β-strand | 293-295 | 3 | 1 |
| β-strand | 299-307 | 9 | 1 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 2 |
| β-strand | 332-336 | 5 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 3 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 378-383 | 6 | 5 |
| β-strand | 386-387 | 2 | 5 |
| β-strand | 391-393 | 3 | 4 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 4 |
| β-strand | 404-413 | 10 | 4 |
| α-helix | 414-419 | 6 | |
| β-strand | 423-428 | 6 | 5 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 6 |
| β-strand | 8 | 1 | 7 |
| β-strand | 17-19 | 3 | 6 |
| β-strand | 25-28 | 4 | 6 |
| β-strand | 48-49 | 2 | 8 |
| β-strand | 50 | 1 | 7 |
| β-strand | 54 | 1 | 8 |
| β-strand | 58-64 | 7 | 6 |
| β-strand | 71-77 | 7 | 8 |
| β-strand | 94-100 | 7 | 8 |
| β-strand | 104-107 | 4 | 8 |
| β-strand | 113-115 | 3 | 8 |
| β-strand | 123-129 | 7 | 6 |
| β-strand | 134-139 | 6 | 6 |
| β-strand | 145-150 | 6 | 6 |
| β-strand | 159-164 | 6 | 8 |
| β-strand | 177-179 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 239-243 | 5 | 9 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-250 | 4 | |
| β-strand | 258-267 | 10 | 9 |
| β-strand | 274-279 | 6 | 10 |
| β-strand | 283-284 | 2 | 10 |
| α-helix | 287 | 1 | |
| β-strand | 288-289 | 2 | 9 |
| α-helix | 290-292 | 3 | |
| β-strand | 293-295 | 3 | 9 |
| β-strand | 299-307 | 9 | 9 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 10 |
| β-strand | 332-336 | 5 | 10 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 11 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 12 |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 12 |
| β-strand | 373 | 1 | 11 |
| β-strand | 378-383 | 6 | 13 |
| β-strand | 386-388 | 3 | 13 |
| β-strand | 391-393 | 3 | 12 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 12 |
| β-strand | 404-413 | 10 | 12 |
| α-helix | 414-419 | 6 | |
| β-strand | 423-428 | 6 | 13 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 14 |
| β-strand | 8 | 1 | 15 |
| β-strand | 17-19 | 3 | 14 |
| β-strand | 25-28 | 4 | 14 |
| β-strand | 48-49 | 2 | 16 |
| β-strand | 50 | 1 | 15 |
| β-strand | 54 | 1 | 16 |
| β-strand | 58-64 | 7 | 14 |
| β-strand | 71-77 | 7 | 16 |
| β-strand | 94-100 | 7 | 16 |
| β-strand | 104-107 | 4 | 16 |
| α-helix | 112 | 1 | |
| β-strand | 113-114 | 2 | 16 |
| β-strand | 123-129 | 7 | 14 |
| β-strand | 134-139 | 6 | 14 |
| β-strand | 145-150 | 6 | 14 |
| β-strand | 159-164 | 6 | 16 |
| α-helix | 169-171 | 3 | |
| α-helix | 175-176 | 2 | |
| β-strand | 177-179 | 3 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-1 chain C | A, D | protein | 207 | HOMO SAPIENS | P01857 (AlphaFold model) |
| 52 kda ro protein | B, E | protein | 181 | HOMO SAPIENS | P19474 (AlphaFold model) |
>2IWG_1 IG GAMMA-1 CHAIN C (chains A, D) GPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQY NSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSR WQQGNVFSCSVMHEALHNHYTQKSLSL
>2IWG_2 52 KDA RO PROTEIN (chains B, E) HMVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYW EVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPP CQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCP L
| ID | Name | Formula | Copies |
|---|---|---|---|
| FUC | alpha-L-fucopyranose | C6 H12 O5 | 2 |
Structural Basis for Pryspry-Mediated Tripartite Motif (Trim) Protein Function. James, L.C., Keeble, A.H., Khan, Z. et al. Proc Natl Acad Sci U S A (2007) 104:6200. DOI 10.1073/PNAS.0609174104 · PubMed
Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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